JPH034785A - Production of sucrose phosphorylase - Google Patents
Production of sucrose phosphorylaseInfo
- Publication number
- JPH034785A JPH034785A JP13477189A JP13477189A JPH034785A JP H034785 A JPH034785 A JP H034785A JP 13477189 A JP13477189 A JP 13477189A JP 13477189 A JP13477189 A JP 13477189A JP H034785 A JPH034785 A JP H034785A
- Authority
- JP
- Japan
- Prior art keywords
- sucrose phosphorylase
- phosphorylase
- medium containing
- lysine
- methionine
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Pending
Links
- 108020000005 Sucrose phosphorylase Proteins 0.000 title claims abstract description 30
- 238000004519 manufacturing process Methods 0.000 title claims description 8
- 150000003839 salts Chemical class 0.000 claims abstract description 9
- 239000004475 Arginine Substances 0.000 claims abstract description 8
- DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 claims abstract description 8
- WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 claims abstract description 8
- AHLPHDHHMVZTML-BYPYZUCNSA-N L-Ornithine Chemical compound NCCC[C@H](N)C(O)=O AHLPHDHHMVZTML-BYPYZUCNSA-N 0.000 claims abstract description 8
- ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 claims abstract description 8
- DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 claims abstract description 8
- CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 claims abstract description 8
- RHGKLRLOHDJJDR-BYPYZUCNSA-N L-citrulline Chemical compound NC(=O)NCCC[C@H]([NH3+])C([O-])=O RHGKLRLOHDJJDR-BYPYZUCNSA-N 0.000 claims abstract description 8
- WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 claims abstract description 8
- ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 claims abstract description 8
- HNDVDQJCIGZPNO-YFKPBYRVSA-N L-histidine Chemical compound OC(=O)[C@@H](N)CC1=CN=CN1 HNDVDQJCIGZPNO-YFKPBYRVSA-N 0.000 claims abstract description 8
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 claims abstract description 8
- FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 claims abstract description 8
- COLNVLDHVKWLRT-QMMMGPOBSA-N L-phenylalanine Chemical compound OC(=O)[C@@H](N)CC1=CC=CC=C1 COLNVLDHVKWLRT-QMMMGPOBSA-N 0.000 claims abstract description 8
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 claims abstract description 8
- 239000004472 Lysine Substances 0.000 claims abstract description 8
- RHGKLRLOHDJJDR-UHFFFAOYSA-N Ndelta-carbamoyl-DL-ornithine Natural products OC(=O)C(N)CCCNC(N)=O RHGKLRLOHDJJDR-UHFFFAOYSA-N 0.000 claims abstract description 8
- AHLPHDHHMVZTML-UHFFFAOYSA-N Orn-delta-NH2 Natural products NCCCC(N)C(O)=O AHLPHDHHMVZTML-UHFFFAOYSA-N 0.000 claims abstract description 8
- UTJLXEIPEHZYQJ-UHFFFAOYSA-N Ornithine Natural products OC(=O)C(C)CCCN UTJLXEIPEHZYQJ-UHFFFAOYSA-N 0.000 claims abstract description 8
- ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 claims abstract description 8
- 235000009697 arginine Nutrition 0.000 claims abstract description 8
- 235000009582 asparagine Nutrition 0.000 claims abstract description 8
- 229960001230 asparagine Drugs 0.000 claims abstract description 8
- 235000003704 aspartic acid Nutrition 0.000 claims abstract description 8
- OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 claims abstract description 8
- 235000013477 citrulline Nutrition 0.000 claims abstract description 8
- 229960002173 citrulline Drugs 0.000 claims abstract description 8
- 235000013922 glutamic acid Nutrition 0.000 claims abstract description 8
- 239000004220 glutamic acid Substances 0.000 claims abstract description 8
- ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 claims abstract description 8
- 235000004554 glutamine Nutrition 0.000 claims abstract description 8
- HNDVDQJCIGZPNO-UHFFFAOYSA-N histidine Natural products OC(=O)C(N)CC1=CN=CN1 HNDVDQJCIGZPNO-UHFFFAOYSA-N 0.000 claims abstract description 8
- 235000018977 lysine Nutrition 0.000 claims abstract description 8
- 229930182817 methionine Natural products 0.000 claims abstract description 8
- 235000006109 methionine Nutrition 0.000 claims abstract description 8
- 229960003104 ornithine Drugs 0.000 claims abstract description 8
- COLNVLDHVKWLRT-UHFFFAOYSA-N phenylalanine Natural products OC(=O)C(N)CC1=CC=CC=C1 COLNVLDHVKWLRT-UHFFFAOYSA-N 0.000 claims abstract description 8
- 238000012258 culturing Methods 0.000 claims abstract description 6
- 244000005700 microbiome Species 0.000 claims description 12
- 150000001242 acetic acid derivatives Chemical class 0.000 claims description 3
- 150000003840 hydrochlorides Chemical class 0.000 claims description 3
- 150000002823 nitrates Chemical class 0.000 claims description 3
- 150000004649 carbonic acid derivatives Chemical class 0.000 claims description 2
- 102000004190 Enzymes Human genes 0.000 abstract description 11
- 108090000790 Enzymes Proteins 0.000 abstract description 11
- 230000000694 effects Effects 0.000 abstract description 6
- 241000894006 Bacteria Species 0.000 abstract description 3
- 239000000126 substance Substances 0.000 abstract 2
- 241000192130 Leuconostoc mesenteroides Species 0.000 abstract 1
- 150000001875 compounds Chemical class 0.000 abstract 1
- 239000000203 mixture Substances 0.000 abstract 1
- 239000002609 medium Substances 0.000 description 15
- 239000000243 solution Substances 0.000 description 11
- 229940088598 enzyme Drugs 0.000 description 10
- 230000002255 enzymatic effect Effects 0.000 description 8
- 235000015097 nutrients Nutrition 0.000 description 7
- 235000002639 sodium chloride Nutrition 0.000 description 7
- 108010073135 Phosphorylases Proteins 0.000 description 6
- 102000009097 Phosphorylases Human genes 0.000 description 6
- 235000001014 amino acid Nutrition 0.000 description 6
- 229940024606 amino acid Drugs 0.000 description 6
- 150000001413 amino acids Chemical class 0.000 description 6
- 239000007788 liquid Substances 0.000 description 6
- 230000001580 bacterial effect Effects 0.000 description 5
- 229960003646 lysine Drugs 0.000 description 5
- CIWBSHSKHKDKBQ-JLAZNSOCSA-N Ascorbic acid Chemical compound OC[C@H](O)[C@H]1OC(=O)C(O)=C1O CIWBSHSKHKDKBQ-JLAZNSOCSA-N 0.000 description 4
- CSNNHWWHGAXBCP-UHFFFAOYSA-L Magnesium sulfate Chemical compound [Mg+2].[O-][S+2]([O-])([O-])[O-] CSNNHWWHGAXBCP-UHFFFAOYSA-L 0.000 description 4
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 4
- 239000000872 buffer Substances 0.000 description 4
- 238000000034 method Methods 0.000 description 4
- BVHLGVCQOALMSV-JEDNCBNOSA-N L-lysine hydrochloride Chemical compound Cl.NCCCC[C@H](N)C(O)=O BVHLGVCQOALMSV-JEDNCBNOSA-N 0.000 description 3
- 241000192132 Leuconostoc Species 0.000 description 3
- HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
- 229930006000 Sucrose Natural products 0.000 description 3
- CZMRCDWAGMRECN-UGDNZRGBSA-N Sucrose Chemical compound O[C@H]1[C@H](O)[C@@H](CO)O[C@@]1(CO)O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 CZMRCDWAGMRECN-UGDNZRGBSA-N 0.000 description 3
- 239000003795 chemical substances by application Substances 0.000 description 3
- 239000001963 growth medium Substances 0.000 description 3
- 239000000758 substrate Substances 0.000 description 3
- 239000005720 sucrose Substances 0.000 description 3
- 241000589220 Acetobacter Species 0.000 description 2
- NLXLAEXVIDQMFP-UHFFFAOYSA-N Ammonia chloride Chemical compound [NH4+].[Cl-] NLXLAEXVIDQMFP-UHFFFAOYSA-N 0.000 description 2
- IJGRMHOSHXDMSA-UHFFFAOYSA-N Atomic nitrogen Chemical compound N#N IJGRMHOSHXDMSA-UHFFFAOYSA-N 0.000 description 2
- VTYYLEPIZMXCLO-UHFFFAOYSA-L Calcium carbonate Chemical compound [Ca+2].[O-]C([O-])=O VTYYLEPIZMXCLO-UHFFFAOYSA-L 0.000 description 2
- BVKZGUZCCUSVTD-UHFFFAOYSA-L Carbonate Chemical compound [O-]C([O-])=O BVKZGUZCCUSVTD-UHFFFAOYSA-L 0.000 description 2
- TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 2
- WCUXLLCKKVVCTQ-UHFFFAOYSA-M Potassium chloride Chemical compound [Cl-].[K+] WCUXLLCKKVVCTQ-UHFFFAOYSA-M 0.000 description 2
- 241000589516 Pseudomonas Species 0.000 description 2
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 2
- 238000002835 absorbance Methods 0.000 description 2
- HXXFSFRBOHSIMQ-VFUOTHLCSA-N alpha-D-glucose 1-phosphate Chemical compound OC[C@H]1O[C@H](OP(O)(O)=O)[C@H](O)[C@@H](O)[C@@H]1O HXXFSFRBOHSIMQ-VFUOTHLCSA-N 0.000 description 2
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 2
- 235000010323 ascorbic acid Nutrition 0.000 description 2
- 239000011668 ascorbic acid Substances 0.000 description 2
- ZCCIPPOKBCJFDN-UHFFFAOYSA-N calcium nitrate Chemical compound [Ca+2].[O-][N+]([O-])=O.[O-][N+]([O-])=O ZCCIPPOKBCJFDN-UHFFFAOYSA-N 0.000 description 2
- 229940041514 candida albicans extract Drugs 0.000 description 2
- 229950010772 glucose-1-phosphate Drugs 0.000 description 2
- BAUYGSIQEAFULO-UHFFFAOYSA-L iron(2+) sulfate (anhydrous) Chemical compound [Fe+2].[O-]S([O-])(=O)=O BAUYGSIQEAFULO-UHFFFAOYSA-L 0.000 description 2
- 229910052943 magnesium sulfate Inorganic materials 0.000 description 2
- 235000019341 magnesium sulphate Nutrition 0.000 description 2
- 229910000402 monopotassium phosphate Inorganic materials 0.000 description 2
- 235000019796 monopotassium phosphate Nutrition 0.000 description 2
- BASFCYQUMIYNBI-UHFFFAOYSA-N platinum Chemical compound [Pt] BASFCYQUMIYNBI-UHFFFAOYSA-N 0.000 description 2
- SCVFZCLFOSHCOH-UHFFFAOYSA-M potassium acetate Chemical compound [K+].CC([O-])=O SCVFZCLFOSHCOH-UHFFFAOYSA-M 0.000 description 2
- GNSKLFRGEWLPPA-UHFFFAOYSA-M potassium dihydrogen phosphate Chemical compound [K+].OP(O)([O-])=O GNSKLFRGEWLPPA-UHFFFAOYSA-M 0.000 description 2
- FGIUAXJPYTZDNR-UHFFFAOYSA-N potassium nitrate Chemical compound [K+].[O-][N+]([O-])=O FGIUAXJPYTZDNR-UHFFFAOYSA-N 0.000 description 2
- LWIHDJKSTIGBAC-UHFFFAOYSA-K potassium phosphate Substances [K+].[K+].[K+].[O-]P([O-])([O-])=O LWIHDJKSTIGBAC-UHFFFAOYSA-K 0.000 description 2
- VWDWKYIASSYTQR-UHFFFAOYSA-N sodium nitrate Chemical compound [Na+].[O-][N+]([O-])=O VWDWKYIASSYTQR-UHFFFAOYSA-N 0.000 description 2
- 239000006228 supernatant Substances 0.000 description 2
- 239000012138 yeast extract Substances 0.000 description 2
- PAWQVTBBRAZDMG-UHFFFAOYSA-N 2-(3-bromo-2-fluorophenyl)acetic acid Chemical compound OC(=O)CC1=CC=CC(Br)=C1F PAWQVTBBRAZDMG-UHFFFAOYSA-N 0.000 description 1
- FRSZYKKDWVPUFP-UHFFFAOYSA-N 2-[3-[(4-amino-2-methylpyrimidin-5-yl)methyl]-4-methyl-1,3-thiazol-3-ium-5-yl]ethyl dihydrogen phosphate;chloride;hydrochloride Chemical compound Cl.[Cl-].CC1=C(CCOP(O)(O)=O)SC=[N+]1CC1=CN=C(C)N=C1N FRSZYKKDWVPUFP-UHFFFAOYSA-N 0.000 description 1
- LXAHHHIGZXPRKQ-UHFFFAOYSA-N 5-fluoro-2-methylpyridine Chemical compound CC1=CC=C(F)C=N1 LXAHHHIGZXPRKQ-UHFFFAOYSA-N 0.000 description 1
- 244000235858 Acetobacter xylinum Species 0.000 description 1
- 235000002837 Acetobacter xylinum Nutrition 0.000 description 1
- 229920001817 Agar Polymers 0.000 description 1
- USFZMSVCRYTOJT-UHFFFAOYSA-N Ammonium acetate Chemical compound N.CC(O)=O USFZMSVCRYTOJT-UHFFFAOYSA-N 0.000 description 1
- 239000005695 Ammonium acetate Substances 0.000 description 1
- NOWKCMXCCJGMRR-UHFFFAOYSA-N Aziridine Chemical compound C1CN1 NOWKCMXCCJGMRR-UHFFFAOYSA-N 0.000 description 1
- UXVMQQNJUSDDNG-UHFFFAOYSA-L Calcium chloride Chemical compound [Cl-].[Cl-].[Ca+2] UXVMQQNJUSDDNG-UHFFFAOYSA-L 0.000 description 1
- OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 description 1
- 101710088194 Dehydrogenase Proteins 0.000 description 1
- 239000003109 Disodium ethylene diamine tetraacetate Substances 0.000 description 1
- ZGTMUACCHSMWAC-UHFFFAOYSA-L EDTA disodium salt (anhydrous) Chemical compound [Na+].[Na+].OC(=O)CN(CC([O-])=O)CCN(CC(O)=O)CC([O-])=O ZGTMUACCHSMWAC-UHFFFAOYSA-L 0.000 description 1
- 229930091371 Fructose Natural products 0.000 description 1
- 239000005715 Fructose Substances 0.000 description 1
- RFSUNEUAIZKAJO-ARQDHWQXSA-N Fructose Chemical compound OC[C@H]1O[C@](O)(CO)[C@@H](O)[C@@H]1O RFSUNEUAIZKAJO-ARQDHWQXSA-N 0.000 description 1
- 239000007836 KH2PO4 Substances 0.000 description 1
- 241000134253 Lanka Species 0.000 description 1
- 102000016943 Muramidase Human genes 0.000 description 1
- 108010014251 Muramidase Proteins 0.000 description 1
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
- 241001282736 Oriens Species 0.000 description 1
- 229910019142 PO4 Inorganic materials 0.000 description 1
- 102000009569 Phosphoglucomutase Human genes 0.000 description 1
- 241000700159 Rattus Species 0.000 description 1
- JZRWCGZRTZMZEH-UHFFFAOYSA-N Thiamine Natural products CC1=C(CCO)SC=[N+]1CC1=CN=C(C)N=C1N JZRWCGZRTZMZEH-UHFFFAOYSA-N 0.000 description 1
- 240000008042 Zea mays Species 0.000 description 1
- 235000005824 Zea mays ssp. parviglumis Nutrition 0.000 description 1
- 235000002017 Zea mays subsp mays Nutrition 0.000 description 1
- XJLXINKUBYWONI-DQQFMEOOSA-N [[(2r,3r,4r,5r)-5-(6-aminopurin-9-yl)-3-hydroxy-4-phosphonooxyoxolan-2-yl]methoxy-hydroxyphosphoryl] [(2s,3r,4s,5s)-5-(3-carbamoylpyridin-1-ium-1-yl)-3,4-dihydroxyoxolan-2-yl]methyl phosphate Chemical compound NC(=O)C1=CC=C[N+]([C@@H]2[C@H]([C@@H](O)[C@H](COP([O-])(=O)OP(O)(=O)OC[C@@H]3[C@H]([C@@H](OP(O)(O)=O)[C@@H](O3)N3C4=NC=NC(N)=C4N=C3)O)O2)O)=C1 XJLXINKUBYWONI-DQQFMEOOSA-N 0.000 description 1
- BXMUVWKVQONWPP-UHFFFAOYSA-N acetic acid sulfane Chemical compound S.CC(O)=O.CC(O)=O BXMUVWKVQONWPP-UHFFFAOYSA-N 0.000 description 1
- 239000008272 agar Substances 0.000 description 1
- 235000019257 ammonium acetate Nutrition 0.000 description 1
- 229940043376 ammonium acetate Drugs 0.000 description 1
- 235000019270 ammonium chloride Nutrition 0.000 description 1
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 1
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 1
- 235000011130 ammonium sulphate Nutrition 0.000 description 1
- 229940072107 ascorbate Drugs 0.000 description 1
- -1 ascorbic acid Chemical class 0.000 description 1
- 229960005070 ascorbic acid Drugs 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- VSGNNIFQASZAOI-UHFFFAOYSA-L calcium acetate Chemical compound [Ca+2].CC([O-])=O.CC([O-])=O VSGNNIFQASZAOI-UHFFFAOYSA-L 0.000 description 1
- 239000001639 calcium acetate Substances 0.000 description 1
- 235000011092 calcium acetate Nutrition 0.000 description 1
- 229960005147 calcium acetate Drugs 0.000 description 1
- 229910000019 calcium carbonate Inorganic materials 0.000 description 1
- 239000001110 calcium chloride Substances 0.000 description 1
- 229910001628 calcium chloride Inorganic materials 0.000 description 1
- 235000011148 calcium chloride Nutrition 0.000 description 1
- 229910052799 carbon Inorganic materials 0.000 description 1
- 235000005822 corn Nutrition 0.000 description 1
- 238000003745 diagnosis Methods 0.000 description 1
- ZPWVASYFFYYZEW-UHFFFAOYSA-L dipotassium hydrogen phosphate Chemical compound [K+].[K+].OP([O-])([O-])=O ZPWVASYFFYYZEW-UHFFFAOYSA-L 0.000 description 1
- 235000019797 dipotassium phosphate Nutrition 0.000 description 1
- 229910000396 dipotassium phosphate Inorganic materials 0.000 description 1
- KCIDZIIHRGYJAE-YGFYJFDDSA-L dipotassium;[(2r,3r,4s,5r,6r)-3,4,5-trihydroxy-6-(hydroxymethyl)oxan-2-yl] phosphate Chemical compound [K+].[K+].OC[C@H]1O[C@H](OP([O-])([O-])=O)[C@H](O)[C@@H](O)[C@H]1O KCIDZIIHRGYJAE-YGFYJFDDSA-L 0.000 description 1
- 235000019301 disodium ethylene diamine tetraacetate Nutrition 0.000 description 1
- 238000005516 engineering process Methods 0.000 description 1
- 238000006911 enzymatic reaction Methods 0.000 description 1
- 239000000284 extract Substances 0.000 description 1
- 239000011790 ferrous sulphate Substances 0.000 description 1
- 235000003891 ferrous sulphate Nutrition 0.000 description 1
- 238000010438 heat treatment Methods 0.000 description 1
- 229910052816 inorganic phosphate Inorganic materials 0.000 description 1
- 229910000358 iron sulfate Inorganic materials 0.000 description 1
- 229910000359 iron(II) sulfate Inorganic materials 0.000 description 1
- 229960005337 lysine hydrochloride Drugs 0.000 description 1
- 235000010335 lysozyme Nutrition 0.000 description 1
- 239000004325 lysozyme Substances 0.000 description 1
- 229960000274 lysozyme Drugs 0.000 description 1
- 229910001629 magnesium chloride Inorganic materials 0.000 description 1
- 235000013372 meat Nutrition 0.000 description 1
- 239000013028 medium composition Substances 0.000 description 1
- 235000013379 molasses Nutrition 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 150000007523 nucleic acids Chemical class 0.000 description 1
- 102000039446 nucleic acids Human genes 0.000 description 1
- 108020004707 nucleic acids Proteins 0.000 description 1
- 239000010452 phosphate Substances 0.000 description 1
- 108091000115 phosphomannomutase Proteins 0.000 description 1
- 239000011574 phosphorus Substances 0.000 description 1
- 229910052698 phosphorus Inorganic materials 0.000 description 1
- 229910052697 platinum Inorganic materials 0.000 description 1
- 229920000642 polymer Polymers 0.000 description 1
- 235000011056 potassium acetate Nutrition 0.000 description 1
- 229960004109 potassium acetate Drugs 0.000 description 1
- 239000001103 potassium chloride Substances 0.000 description 1
- 235000011164 potassium chloride Nutrition 0.000 description 1
- 235000010333 potassium nitrate Nutrition 0.000 description 1
- 239000004323 potassium nitrate Substances 0.000 description 1
- 238000004445 quantitative analysis Methods 0.000 description 1
- 239000011780 sodium chloride Substances 0.000 description 1
- 235000010344 sodium nitrate Nutrition 0.000 description 1
- 239000004317 sodium nitrate Substances 0.000 description 1
- ZNJHFNUEQDVFCJ-UHFFFAOYSA-M sodium;2-[4-(2-hydroxyethyl)piperazin-1-yl]ethanesulfonic acid;hydroxide Chemical compound [OH-].[Na+].OCCN1CCN(CCS(O)(=O)=O)CC1 ZNJHFNUEQDVFCJ-UHFFFAOYSA-M 0.000 description 1
- 241000894007 species Species 0.000 description 1
- 229960003495 thiamine Drugs 0.000 description 1
- 235000019157 thiamine Nutrition 0.000 description 1
- 239000011721 thiamine Substances 0.000 description 1
- KYMBYSLLVAOCFI-UHFFFAOYSA-N thiamine Chemical compound CC1=C(CCO)SCN1CC1=CN=C(C)N=C1N KYMBYSLLVAOCFI-UHFFFAOYSA-N 0.000 description 1
- GPRLSGONYQIRFK-MNYXATJNSA-N triton Chemical compound [3H+] GPRLSGONYQIRFK-MNYXATJNSA-N 0.000 description 1
- 235000013343 vitamin Nutrition 0.000 description 1
- 239000011782 vitamin Substances 0.000 description 1
- 229940088594 vitamin Drugs 0.000 description 1
- 229930003231 vitamin Natural products 0.000 description 1
Landscapes
- Enzymes And Modification Thereof (AREA)
Abstract
Description
【発明の詳細な説明】
〔産業上の利用分野〕
本発明は、シュークロースホスホリラーゼの製造法に関
し、その目的とするところは高酵素活性のシュークロー
スホスホリラーゼを効率良く得ることにある。DETAILED DESCRIPTION OF THE INVENTION [Industrial Application Field] The present invention relates to a method for producing sucrose phosphorylase, and its purpose is to efficiently obtain sucrose phosphorylase with high enzymatic activity.
シュークロースホスホリラーゼは、無機リン酸の存在下
でシェークロースに作用してグルコース−１−リン酸と
フラクトースを生成させる酵素でアリ、ホスホグルコム
ターゼ及びグルコース−６−リン酸デヒドロゲナーゼ等
と組み合わせて、無機リン酸を定量する方法（例えば特
開昭６３−１４６８００号、特開昭６３−４９１００号
公報参照）及びシュークロースの定量分析〔アナライテ
ィカル・バイオケミストリー１４２．５５６〜５６１
（１９８４）３等に適応することができ、診断用酵素剤
等として今後その開発が期待される。Sucrose phosphorylase is an enzyme that acts on sucrose in the presence of inorganic phosphate to produce glucose-1-phosphate and fructose. Methods for quantifying phosphoric acid (see, for example, JP-A-63-146800 and JP-A-63-49100) and quantitative analysis of sucrose [Analytical Biochemistry 142.556-561
(1984) 3, etc., and its development as a diagnostic enzyme agent is expected in the future.
従来、ｐイコノストック属、ンユードモナス属、アセト
バクター属等に属し、ンユークロースホスホリラーゼ生
産能を有する微生物を栄養培地ｔｌＨ１、該培養物より
シュークロースホスホリラーゼを採取する方法が知られ
ている。Conventionally, a method has been known in which a microorganism belonging to the genus P-Iconostoc, Neudomonas, Acetobacter, etc. and having the ability to produce euclose phosphorylase is placed in a nutrient medium tlH1, and sucrose phosphorylase is collected from the culture.
しかしながら、従来の製造法に於いては目的とするシュ
ークロースホスホリラーゼの活性及び収率が低し・欠点
を有し、その改善が強く望まれて（・る。However, conventional production methods have drawbacks such as low activity and yield of the target sucrose phosphorylase, and improvement thereof is strongly desired.
本発明者等は、従来のシュークロースホスホリラーゼの
製造法の上記欠点を解消すべく鋭意検討を重ねた結果、
非常に数多くのアミノ酸類のうち）−ｆ−−にニン、ア
スパラギン、アスパラギン酸、グルタミン、グルタミン
酸、アルギニン、リジン、オルニチン、シトルリン、ヒ
スチジン、フェニルアラニン及びそれらの塩を０．１％
（Ｗ／Ｖ）以上含有する培地に、シュークロースホスホ
リラーゼ生産能を有する微生物を培養したところ、高酵
素活性のシュークロースホスホリラーゼを得ることがで
きること、また該培地に更に炭酸塩、酢酸塩、塩酸塩及
び硝酸塩より選ばれる少なくとも１種を０．０５％（Ｗ
／Ｖ）以上含有させると、著しく高酵素活性のシューク
ロースホスホリラーゼを得ることができることを知り、
これらの知見に基づし・て本発明を完成した。The present inventors have conducted intensive studies to solve the above-mentioned drawbacks of conventional sucrose phosphorylase production methods, and have found that
Among the very large number of amino acids) -f--, 0.1% of nin, asparagine, aspartic acid, glutamine, glutamic acid, arginine, lysine, ornithine, citrulline, histidine, phenylalanine and their salts.
(W/V) When a microorganism capable of producing sucrose phosphorylase is cultured in a medium containing the above, sucrose phosphorylase with high enzymatic activity can be obtained. and 0.05% (W
/V) or more, it is possible to obtain sucrose phosphorylase with extremely high enzymatic activity.
The present invention was completed based on these findings.
即ち本発明はシュークロースホスホリラーゼ生産能を有
する微生物を、メチオニン、アスパラギン、アスパラギ
ン酸、グルタミン、グルタミン酸、アルギニン、リジン
、オルニチン、シトルリン、ヒスチジン、フェニルアラ
ニン及びそれらの塩より選ばれる少なくとも１種を０．
１％（Ｗ／Ｖ）以上含有する培地に培養し、該培養物よ
りンーークジースホスホリラーゼを採取することを特徴
とするシュークロースホスホリラーゼの製造法であり、
また本発明はシュークロースホスホリラーゼ生産能を有
する微生物を、メチオニン、アスパラギン、アスパラギ
ン酸、グルタミン、グルタミン酸、アルギニン、リジン
、オルニチン、シトルリン、ヒスチジン、フェニルアラ
ニン及ヒソレラノ塩より選ばれる少なくとも１種を０．
１％（Ｗ／Ｖ）以上含有し、また炭酸塩、酢酸塩、塩酸
塩及び硝酸塩より選ばれる少なくとも１種を０．０５％
（Ｗ／Ｖ）以上含有する培地に培養し、該培養物よりシ
ュークロースホスホリラーゼを採取することを特徴とス
ルンユークロースホスホリラーゼの製造法である。That is, the present invention uses a microorganism capable of producing sucrose phosphorylase, and at least one selected from methionine, asparagine, aspartic acid, glutamine, glutamic acid, arginine, lysine, ornithine, citrulline, histidine, phenylalanine, and salts thereof at 0.00%.
A method for producing sucrose phosphorylase, which comprises culturing in a medium containing 1% (W/V) or more, and collecting NUC phosphorylase from the culture,
Further, the present invention uses a microorganism capable of producing sucrose phosphorylase in which at least one species selected from methionine, asparagine, aspartic acid, glutamine, glutamic acid, arginine, lysine, ornithine, citrulline, histidine, phenylalanine, and hisorelano salt is added at 0.00%.
Contains 1% (W/V) or more, and 0.05% of at least one selected from carbonates, acetates, hydrochlorides, and nitrates.
(W/V) or more, and sucrose phosphorylase is collected from the culture.
以下、本発明の詳細な説明する。The present invention will be explained in detail below.
本発明に使用されるシュークロースホスホリラーゼ生産
能を有する微生物としては、上記性質を有する微生物で
あれば如何なるものでも良く、例えばロイコノストック
属、シュードモナス属、アセトバクター属に属する微生
物が挙げられる。The microorganism having the ability to produce sucrose phosphorylase used in the present invention may be any microorganism as long as it has the above-mentioned properties, and includes, for example, microorganisms belonging to the genus Leuconostoc, Pseudomonas, and Acetobacter.
上記微生物の具体例としては、例えばロイコノストック
・メツセンチロイデス（ＡＴＣＣ１２２９１）、シュー
ドモナス・サツ力ロフイラ（ＡＴＣＣ１５９４６）、ア
セトバクター・キシリナム（Ｊ、 Ｎａｔｅ、 Ｓｃｉ
。Specific examples of the above-mentioned microorganisms include Leuconostoc metsucentiloides (ATCC 12291), Pseudomonas saturophila (ATCC 15946), Acetobacter xylinum (J, Nate, Sci.
.
Ｃｏｖ−ｃ、 Ｓｒｉ Ｌａｎｋａ １０（２）、 ８
０〜１６９（１９８２）Ｅ等が挙げられる。Cov-c, Sri Lanka 10(2), 8
0-169 (1982) E and the like.
次に上記シュークロースホスホリラーゼ生産能を有する
微生物の培養手段を述べる。Next, a method for culturing the above-mentioned microorganism capable of producing sucrose phosphorylase will be described.
先ず本発明に用いられる培養培地としては、通常の液体
栄養培地に、以下に述べる特定のアミノ酸を添加含有せ
しめた培地が用いられる。First, the culture medium used in the present invention is a normal liquid nutrient medium supplemented with specific amino acids described below.
上記液体栄養培地としては、ンユークロース、糖蜜等の
炭素源、ポリペプトン、酵母エキス、肉エキス、硫酸ア
ンモニウム、コーンステーブリカー等の窒素源、リン酸
１カリウム、リン酸２カリウム、硫酸マグネシウム、硫
酸鉄等の無機塩、チアミン、アスコルビン酸等のビタミ
ンを含有し、ｐ Ｈ６，Ｏ〜８．０に調節したものが好
ましい。The above-mentioned liquid nutrient medium includes carbon sources such as nuclose and molasses, nitrogen sources such as polypeptone, yeast extract, meat extract, ammonium sulfate, and corn stave liquor, monopotassium phosphate, dipotassium phosphate, magnesium sulfate, iron sulfate, etc. Preferably, it contains inorganic salts, thiamine, vitamins such as ascorbic acid, and has a pH adjusted to 6.0 to 8.0.
また、本発明の液体栄養培地に添加されるアミノ酸とし
ては、メチオニン、アスパラギン、アスパラギン酸、グ
ルタミン、グルタミン酸、アルギニン、リジン、オルニ
チン、シトルリン、ヒスチジン、フェニルアラニン及び
それらの塩より選ばれる少なくとも１種が挙げられる。Furthermore, the amino acid added to the liquid nutrient medium of the present invention includes at least one selected from methionine, asparagine, aspartic acid, glutamine, glutamic acid, arginine, lysine, ornithine, citrulline, histidine, phenylalanine, and salts thereof. It will be done.
また、その添加量は培地に対して０．１％（Ｗ／Ｖ）以
上、特に０．３〜２．０％（Ｗ／Ｖ）となるように添加
することが好ましく、又添加時期は培養途中でも良いが
、培地の調整時に添加するのが望ましし・。In addition, it is preferable to add it in an amount of 0.1% (W/V) or more, especially 0.3 to 2.0% (W/V) to the culture medium, and the timing of addition is It can be added midway through, but it is preferable to add it when adjusting the culture medium.
このように、上記のアミノ酸を所定量添加含有せしめた
培地を用いると、高酵素活性のシュークロースホスホリ
ラーゼを効率良く得ることが可能となる。In this way, by using a medium containing a predetermined amount of the above-mentioned amino acids, it becomes possible to efficiently obtain sucrose phosphorylase with high enzymatic activity.
そして、上記培地に対し、炭酸塩、酢酸塩、塩酸塩及び
硝酸塩より選ばれる少なくとも１種を０．０５％（Ｗ／
Ｖ）以上、特ニ０．１〜５％（Ｗ／Ｖ）添加し、培養中
培地のｐＨを５．５〜８． Ｏの範囲に維持するト、更
に高酵素活性のンユークロースホスホリラ〜ゼを効率良
く得ることができるので好ましυ１゜
上記した炭酸塩としては、炭酸カルシウム、炭酸カリウ
ム、炭酸ナトリウム、炭酸アンモニウム等、酢酸塩とし
ては、酢酸すｌ−’Ｊウム、酢酸アンモニウム、酢酸カ
リウム、酢酸カルシウム等、塩酸塩としては塩化ナトリ
ウム、塩化アンモニウム、塩化カルシウム、塩化カリウ
ム等、硝酸塩としては、硝酸ナトリウム、硝酸カリウム
、硝酸アンモニウム、硝酸カルシウム等が好適に用いら
れる。Then, 0.05% (W/
V) Above, add 0.1 to 5% (W/V) and adjust the pH of the medium during culture to 5.5 to 8. It is preferable to maintain the carbonate in the range of 0 and to efficiently obtain nuculose phosphorylase with high enzymatic activity. Acetates include sulfur acetate, ammonium acetate, potassium acetate, calcium acetate, etc. Hydrochlorides include sodium chloride, ammonium chloride, calcium chloride, potassium chloride, etc. Nitrates include sodium nitrate, potassium nitrate, etc. , ammonium nitrate, calcium nitrate, etc. are preferably used.
本発明によれば、定量用酵素剤及び診断用酵素剤として
有用な、高酵素活性のシュークロースホスホリラーゼを
、簡易な操作で、効率良く得ることが出来、産業上極め
て有意義である。According to the present invention, sucrose phosphorylase with high enzymatic activity, which is useful as an enzyme agent for quantitative determination and an enzyme agent for diagnosis, can be obtained efficiently with a simple operation, and is extremely meaningful industrially.
以下、実施例を示して本発明を具体的に説明する。Hereinafter, the present invention will be specifically explained with reference to Examples.
［実 施 例］ 実 施 例 １ ０液体栄養培地組成］ ％は（Ｗ／Ｖ）による。[Example] Implementation example 1 0 Liquid Nutrient Medium Composition] % is based on (W/V).
シェークロース
酵母エキス
ポリペプトン
２．０％
１．０％
１．０％
リン酸２カリウム
チアミン塩酸塩
アスコルビン酸
硫酸マグネシウム
硫酸第１鉄
ＷＬ酎ラマンガ
ン
ｐＨ
１，５％
０．００１％
０．００５％
０．０４％
０．００１％
０．０２％
７．０
（全量Ｌｏｏｍ／）
上記液体栄養培地に、第１表記載の如きアミノ酸を所定
量添加含有した培地１００ ｒａｔを、２００ｍ１容量
の三角フラスコに入れて、１２０°Ｃ１１５分間滅菌し
たものに、肉汁寒天斜面培地にて純粋培養シたロイコノ
ストック・メツセンテロイテス（ＡＴＣＣ１２２９１）
の菌体な３白金耳接種し、これを恒温器で３０℃で１４
時間静置培養した。Shake Rose Yeast Extract Polypeptone 2.0% 1.0% 1.0% Dipotassium Thiamine Phosphate Hydrochloride Ascorbate Magnesium Sulfate Ferrous Sulfate WL Distillery Lamangan pH 1.5% 0.001% 0.005% 0. 04% 0.001% 0.02% 7.0 (Total amount Loom/) Add 100 rats of a medium containing the above liquid nutrient medium and a predetermined amount of amino acids as listed in Table 1 into a 200 ml Erlenmeyer flask. , Leuconostoc metsucenteroites (ATCC12291), which was sterilized at 120°C for 115 minutes and pure cultured on a broth agar slant medium.
Inoculate 3 platinum loops of bacterial cells and incubate at 30°C for 14 days in a thermostat.
The cells were incubated for hours.
このようにして得た培養液４ ｍｌを遠心分離して菌体
を集菌し、得られた菌体を０．０５ Ｍ ＫＨ２ＰＯ４
−ＮａＯＨ緩衝液（ｐＨ６，５）４ｍｇに懸濁し、遠心
分離して洗浄菌体を調製した。4 ml of the culture solution thus obtained was centrifuged to collect the bacterial cells, and the resulting bacterial cells were diluted with 0.05 M KH2PO4.
-The cells were suspended in 4 mg of NaOH buffer (pH 6,5) and centrifuged to prepare washed bacterial cells.
次にこの洗浄菌体をリゾチーム（生化学工業社製）０．
５％（Ｗ／Ｖ）、Ｔｒｉｔｏｎ Ｘ−１０００，１％（
Ｖ／Ｖ）１０ｍＭエチレンジアミン４酢酸２ナトリウム
を含有する０、０５Ｍ ＫＨ２ＰＯ４ＮａＯＨ緩衝液
（ｐＨ６，５）４ｍｇに懸濁した。そして３７°Ｃで３
０分間加温して溶菌し、更にエチレンイミン・ポリマー
（東京化成工業社製）を終濃度が０．００５％（Ｖ／Ｖ
）になるように添加して除核酸を行なったのち、遠心分
離して上清（粗酵素液）を採取した。Next, the washed bacterial cells were washed with 0.0% lysozyme (manufactured by Seikagaku Kogyo Co., Ltd.).
5% (W/V), Triton X-1000, 1% (
V/V) 0.05M KH2PO4NaOH buffer containing 10mM disodium ethylenediaminetetraacetate
(pH 6,5) and suspended in 4 mg. and 3 at 37°C
After heating for 0 minutes to lyse the bacteria, add ethyleneimine polymer (manufactured by Tokyo Kasei Kogyo Co., Ltd.) to a final concentration of 0.005% (V/V
) to remove nucleic acids, and then centrifuged to collect the supernatant (crude enzyme solution).
上清の酵素活性を測定した結果、培養液１ ｍｌ当タリ
のン二−クロースホスホリラーゼ活性は第１表記載の如
くであった。As a result of measuring the enzyme activity of the supernatant, the ni-close phosphorylase activity per 1 ml of the culture solution was as shown in Table 1.
なお、酵素活性の測定は下記の通りである。Note that the enzyme activity was measured as follows.
基質シュークロースを０．０５ Ｍ ＫＨ２ＰＯ４Ｎａ
ＯＨ緩衝液（ｐ Ｈ６，８）中に溶かして基質濃度を１
６０ｍＭに調製する。この基質液３．０コに、前記緩衝
液に溶解した濃度０． ＯＩ Ｍ ＥＤＴＡ−２ナトリ
ウム溶液０．０３ｍＡ、１％（Ｗ／Ｖ） ＮＡＤＰ （
オリエンｐ ｔＩ、酵母社製）溶液０．１ ｍｌ、 ０
．０１％（Ｗ／Ｖ）グルコース−１，６−２リン酸（ヘ
ーリンガーマン・・イム社製）溶液０．１＋ｙ／、１Ｍ
塩化マグネシウムｉ 液０．０５ ｍｅ 、ホスホグル
コムターゼ（ベーリンガーマンハイム社製） ０．０１
ｍｌ 、グルツース−６−リン酸デヒドロゲナーゼ（
オリエンタル酵母社製）０．０１ｍｇを加え、２５゛Ｃ
で約５分間予備加温する。酵素液０．０２ ｍｅを加え
、波長３４０ ｎｍでの１分間当たりの吸光度変化を測
定する。The substrate sucrose was 0.05 M KH2PO4Na.
Dissolve in OH buffer (pH 6,8) to bring the substrate concentration to 1.
Adjust to 60mM. 3.0 of this substrate solution was dissolved in the buffer solution at a concentration of 0.0. OIM EDTA-disodium solution 0.03 mA, 1% (W/V) NADP (
Orien p tI, manufactured by Yeast Co., Ltd.) solution 0.1 ml, 0
．． 01% (W/V) glucose-1,6-2 phosphoric acid (manufactured by Herringermann Im Co.) solution 0.1+y/, 1M
Magnesium chloride i solution 0.05 me, phosphoglucomutase (Boehringer Mannheim) 0.01
ml, gluten-6-phosphate dehydrogenase (
Add 0.01mg (manufactured by Oriental Yeast Co., Ltd.) and heat at 25°C.
Prewarm for about 5 minutes. Add 0.02 me of enzyme solution and measure the change in absorbance per minute at a wavelength of 340 nm.
なおブランク値は、本酵素液０．０２ ｔｎｌの代わり
に０．０１ Ｍ ＨＥＰＥＳ −ＮａＯＨ緩衝液（ｐＨ
７）を０、０２ ｍｌ添加したものである。The blank value is 0.01 M HEPES-NaOH buffer (pH
7) was added in an amount of 0.02 ml.
３３４−０ｎでの酵素反応液及びブランク値の１分間当
たりの吸光度の変化の差より、生成したグルコース−１
−リンＭを定ｔｌ、た。Based on the difference in the absorbance change per minute between the enzyme reaction solution and the blank value at 334-0n, the produced glucose-1
- Phosphorus M was kept at constant tl.
そして力価の表示は２５°Ｃ，１分間当たり１マイクル
モルのグルコース１リン酸を生成する酵素量を１単位と
した。The titer was expressed as 1 unit, which was the amount of enzyme that produced 1 micromole of glucose monophosphate per minute at 25°C.
第１表の結果から、数多くのアミノ酸のうち、メチオニ
ン、アスパラギン、アスパラギン酸、グルタミン、グル
タミン酸、アルギニン、リジン、オルニチン、シトルリ
ン、ヒスチジン、フェニルアラニン及びそれらの塩を単
独又は併用で０．１％（Ｗ／ｖ）以上含有スる培地に、
シュークロースホスホリラーゼ生産能を有する微生物を
培養すると、高酵素活性のシュークロースホスホリラー
ゼが得られることが判る。From the results in Table 1, it was found that among the many amino acids, methionine, asparagine, aspartic acid, glutamine, glutamic acid, arginine, lysine, ornithine, citrulline, histidine, phenylalanine and their salts were used alone or in combination at 0.1% (W /v) or more in a medium containing
It has been found that sucrose phosphorylase with high enzymatic activity can be obtained by culturing microorganisms capable of producing sucrose phosphorylase.
実 施 例 ２
実施例１のシュークロースホスホリラーゼの製造法にお
いて、培地として実施例１の液体栄養培地にリシン塩酸
塩０．５％（Ｗ／Ｖ）及び炭酸カルシウム０．５％（Ｗ
／Ｖ）を添加含有した培地（ｐ Ｈ７，Ｏ）を用いる以
外は全く同様に操作して、３．３５ ｕｙｍｅのンユー
クロースホスホリラーゼ粗酵素液を得た。Example 2 In the method for producing sucrose phosphorylase of Example 1, lysine hydrochloride 0.5% (W/V) and calcium carbonate 0.5% (W/V) were added to the liquid nutrient medium of Example 1 as a medium.
A crude enzyme solution of nuculose phosphorylase of 3.35 uyme was obtained by performing the same procedure except using a medium (pH 7, O) containing 3.35 uyme of nuculose phosphorylase.
第１表及び本実施例の結果から、Ｌ−リジン塩酸塩を０
．５％（Ｗ／Ｖ）添加使用した場合は、１．４８Ｕ／ｍ
ｌのシュークロースホスホリラーゼが得られるが、Ｌ−
リジン塩酸塩０．５％（Ｗ／Ｖ）と炭酸塩０．５％（Ｗ
／Ｖ）を併用添加すると、著しく高酵素活性即ち３．３
５ Ｕ／ａｔのそれが得られることが判る。From Table 1 and the results of this example, it is clear that L-lysine hydrochloride was
．． When using 5% (W/V) addition, 1.48U/m
l of sucrose phosphorylase is obtained, but L-
Lysine hydrochloride 0.5% (W/V) and carbonate 0.5% (W/V)
/V), significantly high enzymatic activity, i.e. 3.3
It can be seen that 5 U/at is obtained.
Claims (2)
生物を、メチオニン、アスパラギン、アスパラギン酸、
グルタミン、グルタミン酸、アルギニン、リジン、オル
ニチン、シトルリン、ヒスチジン、フェニルアラニン及
びそれらの塩より選ばれる少なくとも１種を０．１％（
Ｗ／Ｖ）以上含有する培地に培養し、該培養物よりシュ
ークロースホスホリラーゼを採取することを特徴とする
シュークロースホスホリラーゼの製造法。(1) Microorganisms capable of producing sucrose phosphorylase are used to produce methionine, asparagine, aspartic acid,
0.1% of at least one selected from glutamine, glutamic acid, arginine, lysine, ornithine, citrulline, histidine, phenylalanine and salts thereof (
A method for producing sucrose phosphorylase, which comprises culturing in a medium containing W/V) or more, and collecting sucrose phosphorylase from the culture.
生物を、メチオニン、アスパラギン、アスパラギン酸、
グルタミン、グルタミン酸、アルギニン、リジン、オル
ニチン、シトルリン、ヒスチジン、フェニルアラニン及
びそれらの塩より選ばれる少なくとも１種を０．１（Ｗ
／Ｖ）％以上含有し、また炭酸塩、酢酸塩、塩酸塩及び
硝酸塩より選ばれる少なくとも１種を０．０５％（Ｗ／
Ｖ）以上含有する培地に培養し、該培養物よりシューク
ロースホスホリラーゼを採取することを特徴とするシュ
ークロースホスホリラーゼの製造法。(2) Microorganisms capable of producing sucrose phosphorylase are used to produce methionine, asparagine, aspartic acid,
At least one selected from glutamine, glutamic acid, arginine, lysine, ornithine, citrulline, histidine, phenylalanine and salts thereof at 0.1 (W
/V)% or more, and at least one selected from carbonates, acetates, hydrochlorides, and nitrates at 0.05% (W/V)% or more.
V) A method for producing sucrose phosphorylase, which comprises culturing in a medium containing the above, and collecting sucrose phosphorylase from the culture.
Priority Applications (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP13477189A JPH034785A (en) | 1989-05-30 | 1989-05-30 | Production of sucrose phosphorylase |
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP13477189A JPH034785A (en) | 1989-05-30 | 1989-05-30 | Production of sucrose phosphorylase |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| JPH034785A true JPH034785A (en) | 1991-01-10 |
Family
ID=15136180
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| JP13477189A Pending JPH034785A (en) | 1989-05-30 | 1989-05-30 | Production of sucrose phosphorylase |
Country Status (1)
| Country | Link |
|---|---|
| JP (1) | JPH034785A (en) |
Cited By (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2004108913A1 (en) * | 2003-06-06 | 2004-12-16 | Kao Corporation | Process for producing phosphorylase |
| JP2005013228A (en) * | 2003-06-06 | 2005-01-20 | Kao Corp | Method for producing phosphorylase |
| JP2006084080A (en) * | 2004-09-15 | 2006-03-30 | Max Co Ltd | Ventilation device and ventilation system |
| JP2008113590A (en) * | 2006-11-02 | 2008-05-22 | Univ Kansai | Aminolipid production method |
-
1989
- 1989-05-30 JP JP13477189A patent/JPH034785A/en active Pending
Cited By (6)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO2004108913A1 (en) * | 2003-06-06 | 2004-12-16 | Kao Corporation | Process for producing phosphorylase |
| JP2005013228A (en) * | 2003-06-06 | 2005-01-20 | Kao Corp | Method for producing phosphorylase |
| US7413886B2 (en) | 2003-06-06 | 2008-08-19 | Kao Corporation | Process for producing phosphorylase |
| JP4504739B2 (en) * | 2003-06-06 | 2010-07-14 | 花王株式会社 | Method for producing phosphorylase |
| JP2006084080A (en) * | 2004-09-15 | 2006-03-30 | Max Co Ltd | Ventilation device and ventilation system |
| JP2008113590A (en) * | 2006-11-02 | 2008-05-22 | Univ Kansai | Aminolipid production method |
Similar Documents
| Publication | Publication Date | Title |
|---|---|---|
| KR940005654B1 (en) | Method of producing l-2-amino-4-(hydroxymethyphospinyl)-butylic acid | |
| Bongaerts et al. | Uric acid degradation by Bacillus fastidiosus strains | |
| Halpern et al. | Glutamate transport in wild-type and mutant strains of Escherichia coli | |
| Greenfield et al. | Nonfunctional tricarboxylic acid cycle and the mechanism of glutamate biosynthesis in Acetobacter suboxydans | |
| JPH02117392A (en) | Production of l-2-amino-4-(hydroxymethylphosphinyl) butyric acid | |
| JPS60251895A (en) | Preparation of pyrroloquinoline quinone | |
| JP3301140B2 (en) | Method for producing L-glutamic acid by fermentation method | |
| Matteo et al. | Microbiological studies on the formation of gramicidin S synthetases | |
| EP0120208B1 (en) | Microbiologically produced l-phenylalanin-dehydrogenase, process for obtaining it and its use | |
| JPH034785A (en) | Production of sucrose phosphorylase | |
| JPS59113896A (en) | Preparation of pyrroloquinolinequinone | |
| JPH04135487A (en) | Glucose dehydrogenase and production thereof | |
| JPH04365491A (en) | Production of 4-halo-3-hydroxybutylamide | |
| JP4210325B2 (en) | Theanine production method | |
| Jones et al. | Microbial metabolism of amino alcohols via aldehydes | |
| CA1156570A (en) | Glucose-6-phosphate dehydrogenase and process for preparation thereof | |
| JP3653766B2 (en) | Production method of ε-poly-L-lysine | |
| JPH0223866A (en) | Stabilization of sucrose phosphorylase | |
| JPH02154686A (en) | Production of sucrose phosphorylase | |
| Wagner et al. | Enzymes involved in the assimilation of one-carbon units by Pseudomonas MS | |
| WO1998042863A1 (en) | Highly sensitive method for assaying chiro-inositol and compositions for the assay | |
| McFadden et al. | 3-Phosphoglycerate kinase from Hydrogenomonas facilis | |
| US3408256A (en) | Method of producing 5-amino-4-imidaz-olecarboxamide ribofuranoside by fermentation | |
| Wu et al. | Further studies on the role of phenylalanine in gramicidin S biosynthesis by Bacillus brevis | |
| EP0079792A2 (en) | Process for production of urease |